Article
Expression of glycodelin in human ovarian cancer: immunohistochemistry and possible function
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Published: | March 20, 2006 |
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Glycodelin A (GdA) is primarily produced in endometrial and decidual tissue, although it was also demonstrated in several cancer types, including ovarian serous cancer. GdA acts as a T-cell inhibitor and is involved in inactivation of human monocytes. With a new polyclonal anti-glycodelin antibody, derived from the sequence of human glycodelin and in situ hybridization experiments, the expression of glycodelin in serous, mucinous, endometrioid and clear cell ovarian tumors was demonstrated. A positive immunohistochemical reaction in all forms of epithelium ovarian cancer was observed, which was confirmed by in situ hybridization. Glycodelin is also expressed by granulose cell tumors, a non epithelial form of ovarian cancer. Furthermore, glycodelin was purified from ascites fluid of ovarian cancer patients and from supernatants of the ovarian cancer cell line ovcar-3. Ascites Gd and also ovcar Gd showed differences in its structure of sialyl Lewis type oligosaccharides compared to GdA. Additionally, ascites Gd was demonstrated to be a sufficient inhibitor of the E-selectin mediated HepG2-cell adhesion on immobilized E-selectin with a 102 fold higher potency compared to the monovalent tetrasaccharide sialyl Lewis X but with lower inhibitor potency compared to GdA and serum glycodelin. Another functional assay showed that ascites Gd inhibits IL-2 stimulated proliferation of peripheral blood leucocytes. Therefore, glycodelin could act as an inhibitor of lymphocyte activation and adhesion in ovarian cancer.